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Hsp22 Rabbit mAb#49218

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Product Detail

Product NameHsp22 Rabbit mAb

Clone No.JJ08-53

Host SpeciesRecombinant Rabbit

Clonality Monoclonal

PurificationProA affinity purified

ApplicationsWB, ICC/IF, IHC

Species ReactivityHu, Ms, Rt

Immunogen Descrecombinant protein

ConjugateUnconjugated

Other NamesAlpha crystallin C chain antibody
Alpha-crystallin C chain antibody
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Heat shock 22kDa protein 8 antibody
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Heat shock protein beta 8 antibody
Heat shock protein beta-8 antibody
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HMN 2 antibody
HMN2 antibody
HMN2A antibody
HSB8 antibody
HSPB 8 antibody
HspB8 antibody
HSPB8_HUMAN antibody
OTTHUMP00000239768 antibody
Protein kinase H11 antibody
Small stress protein like protein HSP22 antibody
Small stress protein-like protein HSP22 antibody
Spinal muscular atrophy distal adult autosomal dominant antibody

Accession NoSwiss-Prot#:Q9UJY1

Uniprot Q9UJY1

Gene ID 26353;

Calculated MW22 kDa

Formulation1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.

StorageStore at -20˚C

Application Details
WB: 1:1,000-1:2,000
IHC: 1:50-1:200
ICC: 1:100-1:500

Western blot analysis of Hsp22 on different lysates using anti-Hsp22 antibody at 1/1,000 dilution. Positive control:
Lane 1: HepG2
Lane 2: Mouse skeletal muscle
Immunohistochemical analysis of paraffin-embedded mouse brain tissue using anti-Hsp22 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded rat skeletal muscle tissue using anti-Hsp22 antibody. Counter stained with hematoxylin.
ICC staining Hsp22 in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
ICC staining Hsp22 in A431 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
ICC staining Hsp22 in SH-SY-5Y cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Crystallins are the major proteins expressed in the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b and g families; b and g-crystallins compose a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. a-crystallins consist of three gene products, aA, aB and aC-crystallin, which are members of the small heat shock protein family (HSP20). They are induced by heat shock, and act as molecular chaperones by holding denatured proteins in large soluble aggregates. However, unlike other molecular chaperones, a-crystallins do not renature these proteins. Research indicates that binding occurs between membranes and aC-crystallin. The binding site appears to be at the polar-apolar interface in membrane protein (MIP26) and aC-crystallin; the lipid bilayer becomes less mobile with aC-crystallin binding.

If you have published an article using product 49218, please notify us so that we can cite your literature.

NOTE

Application

  • WBWestern Blotting
  • IHCImmunohistochemistry
  • IFImmunofluorescence
  • ICCImmunocytochemistry
  • FCFlow Cytometry
  • IPImmunoprecipitation
  • EELISA
  • DBDot Blotting
  • ChIPChromatin Immunoprecipitation
  • GICAGold Immunochromatography Assay
  • NCNegative Control

Species Reactivity

  • HuHuman
  • MsMouse
  • RtRat
  • DmDrosophila melanogaster
  • CCaenorhabditis elegans
  • MkMonkey
  • RbRabbit
  • BBovine
  • DDog
  • PPig
  • HmHamster
  • ChHmChinese Hamster
  • ChkChicken
  • ShpSheep
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